Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nicotinate-nucleotide adenylyltransferase

Gene

nadD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).

Catalytic activityi

ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinate-nucleotide adenylyltransferase (nadD)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processPyridine nucleotide biosynthesis
LigandATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU25640-MONOMER
BRENDAi2.7.7.18 658
UniPathwayiUPA00253; UER00332

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinate-nucleotide adenylyltransferase (EC:2.7.7.18)
Alternative name(s):
Deamido-NAD(+) diphosphorylase
Deamido-NAD(+) pyrophosphorylase
Nicotinate mononucleotide adenylyltransferase
Short name:
NaMN adenylyltransferase
Gene namesi
Name:nadD
Synonyms:yqeJ
Ordered Locus Names:BSU25640
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

DrugBankiDB04099 Deamido-Nad+

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001813871 – 189Nicotinate-nucleotide adenylyltransferaseAdd BLAST189

Proteomic databases

PaxDbiP54455
PRIDEiP54455

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100014021

Structurei

Secondary structure

1189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi16 – 28Combined sources13
Beta strandi32 – 38Combined sources7
Beta strandi46 – 48Combined sources3
Helixi53 – 64Combined sources12
Beta strandi70 – 72Combined sources3
Helixi75 – 77Combined sources3
Beta strandi78 – 81Combined sources4
Helixi85 – 95Combined sources11
Beta strandi99 – 106Combined sources8
Turni107 – 112Combined sources6
Beta strandi113 – 116Combined sources4
Helixi117 – 125Combined sources9
Beta strandi126 – 132Combined sources7
Beta strandi145 – 148Combined sources4
Helixi156 – 165Combined sources10
Turni170 – 172Combined sources3
Helixi175 – 183Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KAMX-ray2.10A/B/C/D2-189[»]
1KAQX-ray3.20A/B/C/D/E/F2-189[»]
ProteinModelPortaliP54455
SMRiP54455
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54455

Family & Domainsi

Sequence similaritiesi

Belongs to the NadD family.Curated

Phylogenomic databases

eggNOGiENOG4108Z1W Bacteria
COG1057 LUCA
HOGENOMiHOG000262780
InParanoidiP54455
KOiK00969
OMAiIHIGHLI
PhylomeDBiP54455

Family and domain databases

CDDicd02165 NMNAT, 1 hit
Gene3Di3.40.50.620, 1 hit
HAMAPiMF_00244 NaMN_adenylyltr, 1 hit
InterProiView protein in InterPro
IPR004821 Cyt_trans-like
IPR005248 NadD/NMNAT
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF01467 CTP_transf_like, 1 hit
TIGRFAMsiTIGR00125 cyt_tran_rel, 1 hit
TIGR00482 TIGR00482, 1 hit

Sequencei

Sequence statusi: Complete.

P54455-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIGIFGGT FDPPHNGHLL MANEVLYQAG LDEIWFMPNQ IPPHKQNEDY
60 70 80 90 100
TDSFHRVEML KLAIQSNPSF KLELVEMERE GPSYTFDTVS LLKQRYPNDQ
110 120 130 140 150
LFFIIGADMI EYLPKWYKLD ELLNLIQFIG VKRPGFHVET PYPLLFADVP
160 170 180
EFEVSSTMIR ERFKSKKPTD YLIPDKVKKY VEENGLYES
Length:189
Mass (Da):22,157
Last modified:October 1, 1996 - v1
Checksum:iE2383AA7F0624B95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA Translation: BAA12447.1
AL009126 Genomic DNA Translation: CAB14506.1
PIRiF69951
RefSeqiNP_390442.1, NC_000964.3
WP_004398676.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaiCAB14506; CAB14506; BSU25640
GeneIDi937818
KEGGibsu:BSU25640
PATRICifig|224308.179.peg.2787

Similar proteinsi

Entry informationi

Entry nameiNADD_BACSU
AccessioniPrimary (citable) accession number: P54455
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health